ID W9YMW5_9EURO Unreviewed; 1181 AA.
AC W9YMW5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Prostaglandin-endoperoxide synthase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O1_04122 {ECO:0000313|EMBL:EXJ91015.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ91015.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ91015.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ91015.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ91015.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMWN01000003; EXJ91015.1; -; Genomic_DNA.
DR RefSeq; XP_007723209.1; XM_007725019.1.
DR AlphaFoldDB; W9YMW5; -.
DR STRING; 1182541.W9YMW5; -.
DR GeneID; 19159008; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_1_0_1; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000019484; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd20612; CYP_LDS-like_C; 1.
DR CDD; cd09817; linoleate_diol_synthase_like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR034812; Ppo-like_N.
DR PANTHER; PTHR11903:SF13; LINOLEATE 10R-LIPOXYGENASE; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 2.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019484}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 464
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ SEQUENCE 1181 AA; 134007 MW; 8933BF035C41E33E CRC64;
MPLLRRLSSK FKSNKTAKPD RNDVNRVLTV VTEKAAPLVI GDQTSNSQTV GSSIGQSLEK
TRGVLPSPSS RPLTTVPPPR PSNGEVNSPA TQKDVENLFE EFANLIHASR RPLPTQSGSG
QYLEKEEPSG ILTDLSHLRL NDLKTATHLV EDFLSGEPVD DRQMHMEEVM QLVAALPDRS
STRVNLTSKL LDVLWNSLQH PPMSYMGDKY RYRSADGSNN SFIFPQLGAA NTPYARSVNP
EVVQPGALPD PGLLFDSLLA REEFKPNPNK VSSIFFNWAS LIIHDLFQTD HRDYSISKTS
SYLDLSILYG DTQPDQDMMR TFEQGRIKPD CFAEERLLAF PPACGVMLIM LNRFHNYVVE
QLSLINESGR FDKPSPRLSG DAARLAWKKY DNDLFQTGRL ITCGLYINIT LHDYLRTIVN
LNRTNSTWTL DPRLDRAKTF GDDGTPRGVG NQVSAEFSLS YRWHSCVGEL DEAWTEAVYK
ELFGKPPDEV SLQELMVGLG KYDHELPEDP QQRPFAHLKR NASGKFEDAD LAQIMRTGVE
QVSGAFGARN IPKSMRAITI LGINQSRYWN LCTLNEYRKF FGLKTYDTFE EVNPDPYVAE
QLKHLYEHPD YIELYPGLAI EEYKEPMVPG VGICPTHTIS RVVLSDAVSL VRGDRFYTLD
YGPKGLTSWG YNEVAIDMSV NQGCVFYKLM LRALPDYFKP SSIYAHYPMT IPSENAKIMQ
HLGRYHDYDW SPPAYIPTRV NLTSYKSAKY LLERPKDFTV MWNDGLGFVM GEGGEKFCLG
GDTVFHRKQR ETMHQLIYRD KWHEHVKHFY EYITLRLLHE KSCKIAGINQ VDLTRDVGNL
AHVHFAANIF ALPLKTAENP KGIFSEQELW MAMSVIFTAI FFDFEPTKSF PLRMVAKKLS
TMLGTLIEAN VKTVTATSFV AKLVDGWREN DNALADYGIH MIRRLSETTG MTTSDIAFSH
ILPTACAMVP NQSQVFTQIM DYYLGEEGGK HLPEIQRLAR TNTEESDQLL LRYVNEGIRL
IGTFGSYRRS EVNHVFNDEY TKRRRPVTVK PGDKVFCSFV GAARDPNIFP DPDQVRLDRP
LDSYIHYGVG EHTCLGKEAS MVALTAMLRT VGKLQNLRRA PGPQGQLKKV PRPGGFYVYM
REDQGSYFVF PCTFKVHYDG ELPPLPPVKA EHSYWNDYHR S
//
